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- W107167029 abstract "Publisher Summary This chapter discusses contractile protein isoforms in developing muscle and the nature of the myosin isozymes. The native myosin molecule is composed of two large subunits of molecular weight 200,000 and four small subunits ranging in size from 16 to 27,000. The classic observations of Buller, Eccles and Eccles (1960) showed that developing muscles contract slowly. The ATPase activity of myofibrils from the developing rat EDL muscle is low as compared to the adult value. It has also been shown that the Ca++-activated ATPase of isolated myosin is low in a number of fetal and newborn mammals and increases to the adult values in the perinatal period. The difference between the ATPase values of different myosins is because of the type of heavy chain present and is not determined by the light chains to any significant extent, these earlier results on developing muscles presumably reflect changing heavy chain compositions. The chapter also discusses about studies which suggest that developing muscles might contain a distinct form of myosin, different from either the adult fast or the adult slow type." @default.
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- W107167029 date "1981-01-01" @default.
- W107167029 modified "2023-09-27" @default.
- W107167029 title "CONTRACTILE PROTEIN ISOFORMS IN DEVELOPING MUSCLE: THE NATURE OF THE MYOSIN ISOZYMES" @default.
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- W107167029 doi "https://doi.org/10.1016/b978-0-08-026817-0.50011-1" @default.
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